食品科学 ›› 2005, Vol. 26 ›› Issue (3): 69-71.

• 基础研究 • 上一篇    下一篇

节杆菌β-呋喃果糖苷酶的纯化及性质研究

 童群义, 朱桂兰   

  1. 江南大学食品学院
  • 出版日期:2005-03-15 发布日期:2011-09-19

Purification and Properties of β-fructofuranosidase from Arthrobacter 10137

 TONG  Qun-Yi, ZHU  Gui-Lan   

  1. School of Food Science and Technology, Southern Yangtze University
  • Online:2005-03-15 Published:2011-09-19

摘要: 采用硫酸铵盐析、透析脱盐、Sepharose 6B凝胶色谱等分离纯化技术,从节杆菌培养液分离纯化了β-呋喃果糖苷酶,纯化倍数为18.29,回收率为44.81%,经SDS-聚丙烯酰胺凝胶电泳后有一条明显的蛋白质谱带。相对分子量为55800左右,该酶的最适pH为6.5,最适温度为30℃,在pH 6.0~8.0之间和45℃以下稳定,Ag+和Cu2+对该酶有较强烈的抑制作用,EDTA和镁离子对酶活的影响较小。

关键词: 节杆菌, &beta, -呋喃果糖苷酶, 纯化和性质

Abstract: The crudeβ-fructofuranosidase prepared from Arthrobacter sp. 10137 was fractioned in a sequence of operations including ammonium sulfate fraction, dialysis and column chromatography with Sepharose 6B. Purification of about 18.29 fold was achieved with an overall yield of 44.81%. The pure enzyme showed a single protein band by SDS-PAGE. Its molecular weight was estimated to be about 55800 by SDS-PAGE. The optimum temperature and pH of the enzyme were 30℃ and 6.5 respectively. The enzyme was stable under 45℃ in the range of pH 6.0~8.0. The Ag+ and Cu2+ strongly inhibited β- fructofuranosidase activity, while EDTA and Mg2+ had no significant effect on it.

Key words: Arthrobacter 10137, β-fructofuranosidase, purification, properties